Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P32327

- PYC2_YEAST

UniProt

P32327 - PYC2_YEAST

Protein

Pyruvate carboxylase 2

Gene

PYC2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.

    Catalytic activityi

    ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate.

    Cofactori

    Biotin.
    Zinc.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei137 – 1371ATPBy similarity
    Binding sitei221 – 2211ATPBy similarity
    Binding sitei256 – 2561ATPBy similarity
    Active sitei313 – 3131By similarity
    Metal bindingi567 – 5671Divalent metal cationBy similarity
    Binding sitei639 – 6391SubstrateBy similarity
    Metal bindingi735 – 7351Divalent metal cation; via carbamate groupBy similarity
    Metal bindingi765 – 7651Divalent metal cationBy similarity
    Metal bindingi767 – 7671Divalent metal cationBy similarity
    Binding sitei899 – 8991SubstrateBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. biotin carboxylase activity Source: InterPro
    3. DNA binding Source: InterPro
    4. metal ion binding Source: UniProtKB-KW
    5. pyruvate carboxylase activity Source: SGD

    GO - Biological processi

    1. gluconeogenesis Source: SGD

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Gluconeogenesis

    Keywords - Ligandi

    ATP-binding, Biotin, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:YBR218C-MONOMER.
    BRENDAi6.4.1.1. 984.
    ReactomeiREACT_188404. Defective HLCS causes multiple carboxylase deficiency.
    REACT_188774. Biotin transport and metabolism.
    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate carboxylase 2 (EC:6.4.1.1)
    Alternative name(s):
    Pyruvic carboxylase 2
    Short name:
    PCB 2
    Gene namesi
    Name:PYC2
    Ordered Locus Names:YBR218C
    ORF Names:YBR1507
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR218c.
    SGDiS000000422. PYC2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 11801179Pyruvate carboxylase 2PRO_0000146825Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei735 – 7351N6-carboxylysineBy similarity
    Modified residuei1136 – 11361N6-biotinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP32327.
    PaxDbiP32327.
    PeptideAtlasiP32327.

    Expressioni

    Inductioni

    By glucose.

    Gene expression databases

    GenevestigatoriP32327.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi32915. 86 interactions.
    DIPiDIP-6426N.
    IntActiP32327. 2 interactions.
    MINTiMINT-2781496.
    STRINGi4932.YBR218C.

    Structurei

    3D structure databases

    ProteinModelPortaliP32327.
    SMRiP32327. Positions 22-1170.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 471453Biotin carboxylationAdd
    BLAST
    Domaini141 – 338198ATP-graspPROSITE-ProRule annotationAdd
    BLAST
    Domaini558 – 825268CarboxyltransferaseAdd
    BLAST
    Domaini1102 – 116968Biotinyl-bindingAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni566 – 5705Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
    Contains 1 biotin carboxylation domain.Curated
    Contains 1 biotinyl-binding domain.Curated
    Contains 1 carboxyltransferase domain.Curated

    Phylogenomic databases

    eggNOGiCOG1038.
    GeneTreeiENSGT00750000118625.
    HOGENOMiHOG000282801.
    KOiK01958.
    OMAiGPTADTM.
    OrthoDBiEOG7GQZ41.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    3.20.20.70. 1 hit.
    3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR003379. Carboxylase_cons_dom.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR009057. Homeodomain-like.
    IPR016185. PreATP-grasp_dom.
    IPR000891. PYR_CT.
    IPR005930. Pyruv_COase.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PANTHERiPTHR18866:SF10. PTHR18866:SF10. 1 hit.
    PfamiPF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    PF00682. HMGL-like. 1 hit.
    PF02436. PYC_OADA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001594. Pyruv_carbox. 1 hit.
    SMARTiSM00878. Biotin_carb_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    TIGRFAMsiTIGR01235. pyruv_carbox. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00866. CPSASE_1. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    PS50991. PYR_CT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P32327-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSKKLAGL RDNFSLLGEK NKILVANRGE IPIRIFRSAH ELSMRTIAIY     50
    SHEDRLSMHR LKADEAYVIG EEGQYTPVGA YLAMDEIIEI AKKHKVDFIH 100
    PGYGFLSENS EFADKVVKAG ITWIGPPAEV IDSVGDKVSA RHLAARANVP 150
    TVPGTPGPIE TVQEALDFVN EYGYPVIIKA AFGGGGRGMR VVREGDDVAD 200
    AFQRATSEAR TAFGNGTCFV ERFLDKPKHI EVQLLADNHG NVVHLFERDC 250
    SVQRRHQKVV EVAPAKTLPR EVRDAILTDA VKLAKVCGYR NAGTAEFLVD 300
    NQNRHYFIEI NPRIQVEHTI TEEITGIDIV SAQIQIAAGA TLTQLGLLQD 350
    KITTRGFSIQ CRITTEDPSK NFQPDTGRLE VYRSAGGNGV RLDGGNAYAG 400
    ATISPHYDSM LVKCSCSGST YEIVRRKMIR ALIEFRIRGV KTNIPFLLTL 450
    LTNPVFIEGT YWTTFIDDTP QLFQMVSSQN RAQKLLHYLA DLAVNGSSIK 500
    GQIGLPKLKS NPSVPHLHDA QGNVINVTKS APPSGWRQVL LEKGPSEFAK 550
    QVRQFNGTLL MDTTWRDAHQ SLLATRVRTH DLATIAPTTA HALAGAFALE 600
    CWGGATFDVA MRFLHEDPWE RLRKLRSLVP NIPFQMLLRG ANGVAYSSLP 650
    DNAIDHFVKQ AKDNGVDIFR VFDALNDLEQ LKVGVNAVKK AGGVVEATVC 700
    YSGDMLQPGK KYNLDYYLEV VEKIVQMGTH ILGIKDMAGT MKPAAAKLLI 750
    GSLRTRYPDL PIHVHSHDSA GTAVASMTAC ALAGADVVDV AINSMSGLTS 800
    QPSINALLAS LEGNIDTGIN VEHVRELDAY WAEMRLLYSC FEADLKGPDP 850
    EVYQHEIPGG QLTNLLFQAQ QLGLGEQWAE TKRAYREANY LLGDIVKVTP 900
    TSKVVGDLAQ FMVSNKLTSD DIRRLANSLD FPDSVMDFFE GLIGQPYGGF 950
    PEPLRSDVLR NKRRKLTCRP GLELEPFDLE KIREDLQNRF GDIDECDVAS 1000
    YNMYPRVYED FQKIRETYGD LSVLPTKNFL APAEPDEEIE VTIEQGKTLI 1050
    IKLQAVGDLN KKTGQREVYF ELNGELRKIR VADKSQNIQS VAKPKADVHD 1100
    THQIGAPMAG VIIEVKVHKG SLVKKGESIA VLSAMKMEMV VSSPADGQVK 1150
    DVFIKDGESV DASDLLVVLE EETLPPSQKK 1180
    Length:1,180
    Mass (Da):130,167
    Last modified:October 1, 1994 - v2
    Checksum:iAD60DA3A60F5E001
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151S → C in CAA42544. (PubMed:1921979)Curated
    Sequence conflicti132 – 1321D → E in CAA42544. (PubMed:1921979)Curated
    Sequence conflicti238 – 2381N → K in CAA42544. (PubMed:1921979)Curated
    Sequence conflicti268 – 2681L → F in CAA42544. (PubMed:1921979)Curated
    Sequence conflicti546 – 5461S → C in CAA42544. (PubMed:1921979)Curated
    Sequence conflicti642 – 6421N → T in CAA42544. (PubMed:1921979)Curated
    Sequence conflicti771 – 7733GTA → STR in CAA42544. (PubMed:1921979)Curated
    Sequence conflicti831 – 8311W → R in CAA42544. (PubMed:1921979)Curated
    Sequence conflicti839 – 8391S → P in CAA42544. (PubMed:1921979)Curated
    Sequence conflicti1001 – 10011Y → N in CAA42544. (PubMed:1921979)Curated
    Sequence conflicti1155 – 11551K → R in CAA42544. (PubMed:1921979)Curated
    Sequence conflicti1178 – 11781Q → P in CAA42544. (PubMed:1921979)Curated
    Sequence conflicti1180 – 11801K → KVIFTR in CAA42544. (PubMed:1921979)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59890 Genomic DNA. Translation: CAA42544.1.
    U35647 Genomic DNA. Translation: AAC49147.1.
    Z36087 Genomic DNA. Translation: CAA85182.1.
    BK006936 Genomic DNA. Translation: DAA07334.1.
    PIRiS46094.
    RefSeqiNP_009777.1. NM_001178566.1.

    Genome annotation databases

    EnsemblFungiiYBR218C; YBR218C; YBR218C.
    GeneIDi852519.
    KEGGisce:YBR218C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59890 Genomic DNA. Translation: CAA42544.1 .
    U35647 Genomic DNA. Translation: AAC49147.1 .
    Z36087 Genomic DNA. Translation: CAA85182.1 .
    BK006936 Genomic DNA. Translation: DAA07334.1 .
    PIRi S46094.
    RefSeqi NP_009777.1. NM_001178566.1.

    3D structure databases

    ProteinModelPortali P32327.
    SMRi P32327. Positions 22-1170.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32915. 86 interactions.
    DIPi DIP-6426N.
    IntActi P32327. 2 interactions.
    MINTi MINT-2781496.
    STRINGi 4932.YBR218C.

    Proteomic databases

    MaxQBi P32327.
    PaxDbi P32327.
    PeptideAtlasi P32327.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR218C ; YBR218C ; YBR218C .
    GeneIDi 852519.
    KEGGi sce:YBR218C.

    Organism-specific databases

    CYGDi YBR218c.
    SGDi S000000422. PYC2.

    Phylogenomic databases

    eggNOGi COG1038.
    GeneTreei ENSGT00750000118625.
    HOGENOMi HOG000282801.
    KOi K01958.
    OMAi GPTADTM.
    OrthoDBi EOG7GQZ41.

    Enzyme and pathway databases

    UniPathwayi UPA00138 .
    BioCyci YEAST:YBR218C-MONOMER.
    BRENDAi 6.4.1.1. 984.
    Reactomei REACT_188404. Defective HLCS causes multiple carboxylase deficiency.
    REACT_188774. Biotin transport and metabolism.

    Miscellaneous databases

    NextBioi 971553.

    Gene expression databases

    Genevestigatori P32327.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    3.20.20.70. 1 hit.
    3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR003379. Carboxylase_cons_dom.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR009057. Homeodomain-like.
    IPR016185. PreATP-grasp_dom.
    IPR000891. PYR_CT.
    IPR005930. Pyruv_COase.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    PANTHERi PTHR18866:SF10. PTHR18866:SF10. 1 hit.
    Pfami PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    PF00682. HMGL-like. 1 hit.
    PF02436. PYC_OADA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001594. Pyruv_carbox. 1 hit.
    SMARTi SM00878. Biotin_carb_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    TIGRFAMsi TIGR01235. pyruv_carbox. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00866. CPSASE_1. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    PS50991. PYR_CT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequences in chromosomes II and VII code for pyruvate carboxylase isoenzymes in Saccharomyces cerevisiae: analysis of pyruvate carboxylase-deficient strains."
      Stucka R., Dequin S., Salmon J.-M., Gancedo C.
      Mol. Gen. Genet. 229:307-315(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    2. "Polymorphism of the yeast pyruvate carboxylase 2 gene and protein: effects on protein biotinylation."
      Val D.L., Chapman-Smith A., Walker M.E., Cronan J.E. Jr., Wallace J.C.
      Biochem. J. 312:817-825(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPYC2_YEAST
    AccessioniPrimary (citable) accession number: P32327
    Secondary accession number(s): D6VQL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 17000 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3